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TRAIL (TNF-RELATED APOPTOSIS INDUCING LIGAND)
Name: Marissa McGarry 03/02/09 LKT: 13 beta STRANDS

The overall structure of TRAIL is a set of 13 beta sheets (shown in red). As you can see, the exterior of the protein has all of the negative and positive side chains, as shown in pink. The amphipathic elements on the surface of the protein are shown on the beta sheets in green. The polar/charged elements are on the surface of the protein, while the hydrophobic elements are on the inside of the beta sheet. Phe181, shown in green, is a hydrophobic element on the surface of the protein.

TRAIL is a member of the tumor necrosis factor(TNF) family. TRAIL selectively induces apoptosis in a wide variety of tumor cells but not in normal cells, which gives it promise as a cancer therapeutic.

"To help in elucidating its biological roles and designing mutants with improved therapeutic potential, we have determined the crystal structure of human TRAIL. The structure reveals that a unique frame insertion of 12-16 amino acids adopts a salient loop structure penetrating into the receptor-binding site. The loop drastically alters the common receptor-binding surface of the TNF family most likely for the specific recognition of cognate partners. A structure-based mutagenesis study demonstrates a critical role of the insertion loop in the cytotoxic activity of TRAIL."

Reference: 1d2q proteopedia page